Authors: Burakova, Ekaterina
Vasa, Suresh K.
Linser, Rasmus
Title: Characterization of conformational heterogeneity via higher-dimensionality, proton-detected solid-state NMR
Language (ISO): en
Abstract: Site-specific heterogeneity of solid protein samples can be exploited as valuable information to answer biological questions ranging from thermodynamic properties determining fibril formation to protein folding and conformational stability upon stress. In particular, for proteins of increasing molecular weight, however, site-resolved assessment without residue-specific labeling is challenging using established methodology, which tends to rely on carbon-detected 2D correlations. Here we develop purely chemical-shift-based approaches for assessment of relative conformational heterogeneity that allows identification of each residue via four chemical-shift dimensions. High dimensionality diminishes the probability of peak overlap in the presence of multiple, heterogeneously broadened resonances. Utilizing backbone dihedral-angle reconstruction from individual contributions to the peak shape either via suitably adapted prediction routines or direct association with a relational database, the methods may in future studies afford assessment of site-specific heterogeneity of proteins without site-specific labeling.
Subject Headings: Fast-MAS solid-state NMR
Proton detection
Sample heterogeneity
Issue Date: 2022-09-23
Rights link:
Appears in Collections:Physikalische Chemie

Files in This Item:
File Description SizeFormat 
s10858-022-00405-0.pdfDNB2.04 MBAdobe PDFView/Open

This item is protected by original copyright

This item is licensed under a Creative Commons License Creative Commons